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Originally published In Press as doi:10.1074/jbc.C200132200 on March 29, 2002

J. Biol. Chem., Vol. 277, Issue 22, 19243-19246, May 31, 2002
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ACCELERATED PUBLICATION
Substrate Recognition Drives the Evolution of Serine Proteases*

Thierry Rose and Enrico Di CeraDagger

From the Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri 63110

A method is introduced to identify amino acid residues that dictate the functional diversity acquired during evolution in a protein family. Using over 80 enzymes of the chymotrypsin family, we demonstrate that the general organization of the phylogenetic tree and its functional branch points are fully accounted for by a limited number of residues that cluster around the active site of the protein and define the contact region with the P1-P4 residues of substrate.

* This work was supported in part by National Institutes of Health Research Grants HL49413 and HL58141.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Box 8231, 660 S. Euclid Ave., St. Louis, MO 63110. Tel.: 314-362-4185; Fax: 314-747-5354; E-mail: enrico@biochem.wustl.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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